Optimization of enzymatic hydrolysis conditions of seaweed (Gracilaria fisheri) protein by using Alcalase® to obtain maximum angiotensin-I-converting enzyme (ACE) inhibitory activity

This study aimed to optimize the enzymatic hydrolysis conditions of Gracilaria fisheri protein by using Alcalase® to obtain maximum angiotensin-I-converting enzyme (ACE) inhibitory activity. Firstly, the seaweed protein was extracted using cellulase, sonication, and ammonium sulphate treatment, be...

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Main Authors: Amiza Mat Amin, Wong, Sher Lee, Kazi Nazira Sharmin
Format: Article
Language:English
Published: Penerbit Universiti Kebangsaan Malaysia 2020
Online Access:http://journalarticle.ukm.my/17389/
http://journalarticle.ukm.my/17389/1/49_05_11.pdf
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author Amiza Mat Amin,
Wong, Sher Lee
Kazi Nazira Sharmin,
author_facet Amiza Mat Amin,
Wong, Sher Lee
Kazi Nazira Sharmin,
author_sort Amiza Mat Amin,
building UKM Institutional Repository
collection Online Access
description This study aimed to optimize the enzymatic hydrolysis conditions of Gracilaria fisheri protein by using Alcalase® to obtain maximum angiotensin-I-converting enzyme (ACE) inhibitory activity. Firstly, the seaweed protein was extracted using cellulase, sonication, and ammonium sulphate treatment, before dialysis and lyophilization. The yield of lyophilized seaweed protein extract was 8.75% with a protein content of 66.4%. An optimization study for protein hydrolysis condition was performed by employing a three-level face-centered central composite design (CCD) using Design-Expert software. Four parameters used were pH (6.5 – 8.5), temperature (50 – 60°C), hydrolysis time (60 – 180 min), and Alcalase® to substrate ratio (E/S) (1.25 – 2.50%). Thirty runs of protein hydrolysis conditions with 6 center points were employed. The supernatant of the resulting protein hydrolysates was then lyophilized and analyzed for ACE inhibitory activity. This study found that the quadratic model could be used to explain the relationship between hydrolysis conditions of G. fisheri protein and ACE inhibitory activity. The optimum condition to obtain maximum ACE inhibitory activity was at pH of 7.5, the temperature of 54.6°C, hydrolysis time of 175 min, and E/S of 1.47%. The half-maximal inhibitory concentration (IC50) of the seaweed protein hydrolysate at optimum condition was 2.97 ± 0.37 mg/mL.
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spelling oai:generic.eprints.org:173892021-08-30T03:57:16Z http://journalarticle.ukm.my/17389/ Optimization of enzymatic hydrolysis conditions of seaweed (Gracilaria fisheri) protein by using Alcalase® to obtain maximum angiotensin-I-converting enzyme (ACE) inhibitory activity Amiza Mat Amin, Wong, Sher Lee Kazi Nazira Sharmin, This study aimed to optimize the enzymatic hydrolysis conditions of Gracilaria fisheri protein by using Alcalase® to obtain maximum angiotensin-I-converting enzyme (ACE) inhibitory activity. Firstly, the seaweed protein was extracted using cellulase, sonication, and ammonium sulphate treatment, before dialysis and lyophilization. The yield of lyophilized seaweed protein extract was 8.75% with a protein content of 66.4%. An optimization study for protein hydrolysis condition was performed by employing a three-level face-centered central composite design (CCD) using Design-Expert software. Four parameters used were pH (6.5 – 8.5), temperature (50 – 60°C), hydrolysis time (60 – 180 min), and Alcalase® to substrate ratio (E/S) (1.25 – 2.50%). Thirty runs of protein hydrolysis conditions with 6 center points were employed. The supernatant of the resulting protein hydrolysates was then lyophilized and analyzed for ACE inhibitory activity. This study found that the quadratic model could be used to explain the relationship between hydrolysis conditions of G. fisheri protein and ACE inhibitory activity. The optimum condition to obtain maximum ACE inhibitory activity was at pH of 7.5, the temperature of 54.6°C, hydrolysis time of 175 min, and E/S of 1.47%. The half-maximal inhibitory concentration (IC50) of the seaweed protein hydrolysate at optimum condition was 2.97 ± 0.37 mg/mL. Penerbit Universiti Kebangsaan Malaysia 2020 Article PeerReviewed application/pdf en http://journalarticle.ukm.my/17389/1/49_05_11.pdf Amiza Mat Amin, and Wong, Sher Lee and Kazi Nazira Sharmin, (2020) Optimization of enzymatic hydrolysis conditions of seaweed (Gracilaria fisheri) protein by using Alcalase® to obtain maximum angiotensin-I-converting enzyme (ACE) inhibitory activity. Malaysian Applied Biology, 49 (5). pp. 99-113. ISSN 0126-8643 http://www.mabjournal.com/index.php?option=com_content&view=article&id=1078&catid=59:current-view&Itemid=56
spellingShingle Amiza Mat Amin,
Wong, Sher Lee
Kazi Nazira Sharmin,
Optimization of enzymatic hydrolysis conditions of seaweed (Gracilaria fisheri) protein by using Alcalase® to obtain maximum angiotensin-I-converting enzyme (ACE) inhibitory activity
title Optimization of enzymatic hydrolysis conditions of seaweed (Gracilaria fisheri) protein by using Alcalase® to obtain maximum angiotensin-I-converting enzyme (ACE) inhibitory activity
title_full Optimization of enzymatic hydrolysis conditions of seaweed (Gracilaria fisheri) protein by using Alcalase® to obtain maximum angiotensin-I-converting enzyme (ACE) inhibitory activity
title_fullStr Optimization of enzymatic hydrolysis conditions of seaweed (Gracilaria fisheri) protein by using Alcalase® to obtain maximum angiotensin-I-converting enzyme (ACE) inhibitory activity
title_full_unstemmed Optimization of enzymatic hydrolysis conditions of seaweed (Gracilaria fisheri) protein by using Alcalase® to obtain maximum angiotensin-I-converting enzyme (ACE) inhibitory activity
title_short Optimization of enzymatic hydrolysis conditions of seaweed (Gracilaria fisheri) protein by using Alcalase® to obtain maximum angiotensin-I-converting enzyme (ACE) inhibitory activity
title_sort optimization of enzymatic hydrolysis conditions of seaweed (gracilaria fisheri) protein by using alcalase® to obtain maximum angiotensin-i-converting enzyme (ace) inhibitory activity
url http://journalarticle.ukm.my/17389/
http://journalarticle.ukm.my/17389/
http://journalarticle.ukm.my/17389/1/49_05_11.pdf